Mac 387 antibody and detection of formalin resistant myelomonocytic LI antigen - Journal of Clinical Pathology
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J Clin Pathol: first published as 10.1136/jcp.41.9.963 on 1 September 1988. Downloaded from http://jcp.bmj.com/ on August 31, 2023 by guest. Protected by
J Clin Pathol 1988;41:963-970
Mac 387 antibody and detection of formalin resistant
myelomonocytic LI antigen
P BRANDTZAEG,* D B JONES,f D J FLAVELL,t M K FAGERHOLI
From the *Laboratoryfor Immunohistochemistry and Immunopathology (LIIPA T), Institute of Pathology,
University of Oslo, The National Hospital, Rikshospitalet, Oslo, Norway, the t University Department of
Pathology, Southampton General Hospital, Southampton, and the lBlood Bank and Department of Immunology,
Ulleval Hospital, Oslo, Norway
suMMARY The murine monoclonal antibody Mac 387 was raised against a purified protein fraction
obtained from human monocytes. By immunoblotting experiments, Mac 387 was shown to react with
a previously defined antigen called LI; this is a multichain myelomoncytic protein of about 36 Kd
which shows sequence homology with the cystic fibrosis antigen. The LI protein is present in the
cytoplasm of virtually all resting peripheral neutrophils and monocytes; it is also variably expressed
on the plasma membrane of these cells, possibly as a secretory product. Because the LI antigen is
resistant to denaturation by formalin, its tissue distribution can be studied in routinely processed
biopsy material. In a wide variety of specimens Mac 387 was shown by immunohistochemical
analysis, to produce a cytoplasmic staining pattern concordant with that of a well defined polyclonal
antibody to the LI antigen. Cytoplasmic reactivity was obtained with granulocytes and infiltrating
macrophages but generally not with several categories of dendritic cells. In addition, squamous
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epithelium of mucous membranes was strongly positive, in contrast to normal epidermis.
The human LI antigen is a multichain protein of about various skin tumours.9 Moreover, mucosal squamous
36 Kd first isolated from granulocytes; it binds calcium epithelium normally expresses Ll'
ions avidly and shows a striking heterogeneity on A rabbit antiserum S22, raised against human
isoelectric focusing.' Like lysozyme and myeloper- monocytes showed some similarities to anti-LI when
oxidase, LI occurs in both circulating neutrophils and tested by immunohistochemical techniques.'" The S22-
monocytes.2 It is of interest that the Ll-light chain related antigens, however, were found to be expressed
shows sequence homology with the cystic fibrosis by Kupffer cells in normal livers and also by inter-
antigen,34 and the two LI chains seem to be identical digitating cells. A similarly prepared antiserum S42
with the recently described macrophage migration was recently used to capture detergent-solubilised
inhibitory factor (MIF)-related proteins MRP-8 and monocyte proteins which were then used to raise a
MRP-14.35 murine monoclonal antibody." This study aimed to
The LI antigen is remarkably well preserved in show that Mac 387 is specific for the well defined Ll
formalin fixed and paraffin wax embedded routine antigen.
biopsy material.6 LI shows a restricted distribution
within the monocyte-derived cell lineage, being mainly Material and methods
confined to reactive histiocytes (infiltrating macro-
phages). It is usually lacking in HLA-DR positive A variety of biopsy specimens were obtained from the
interdigitating cells, Langerhans' cells, intestinal his- routine pathology files.6 This material had been fixed
tiocytes, Kupffer cells of normal livers, and follicular in buffered formalin (pH 7.4) and embedded in
dendritic cells.6 A protein sharing physicochemical paraffin wax. A similar selection of tissue was obtained
and antigenic properties with LI has been identified as fresh material and prepared by direct ethanol
in psoriatic epidermal extracts.7 It is generally not fixation at 4°C followed by paraffin wax embedding
expressed by normal epidermis but is abundant in according to the method of Sainte-Marie.'2
several inflammatory skin diseases8 and adjacent to
PRIMARY ANTIBODY REAGENTS FOR
IMMUNOHISTOCHEMISTRY
Accepted for publication 7 April 1988 Production and characterisation of monoclonal Mac
963J Clin Pathol: first published as 10.1136/jcp.41.9.963 on 1 September 1988. Downloaded from http://jcp.bmj.com/ on August 31, 2023 by guest. Protected by
964 Brandtzaeg, Jones, Flavell, Fagerhol
387 have been detailed elsewhere." Fluorescein and hours at room temperature. Thereafter incubation
rhodamine conjugates were prepared from took place overnight with peroxidase-labelled goat
appropriately absorbed antisera with various anti-rabbit or anti-mouse IgG conjugate at 1/1000
specificities, including anti-L i' 13 14 A rabbit antiserum (Bio-Rad). The enzyme substrate was diamino-
to S- 100 protein (A588, Dako, USA) was used to label benzidine in 0-1 M sodium citrate, pH 5, with 0-015%
Langerhans' and interdigitating cells.'5 All antibody H202.
incubations took place at room temperature for 30 Dot blot experiments were performed with crude
minutes or 20 hours; the reagents were appropriately leucocyte extract containing a known amount of LI
diluted in isotonic phosphate buffered saline (PBS), antigen and with two fractions of purified LI protein.'
pH 7*5, containing bovine serum albumin (BSA) at After application of the samples (1 p1) in two-fold
125 g/l. serial dilutions (representing from 2000 to 0-2 ng LI
antigen), the nitrocellulose sheets were soaked in
IMMUNOENZYME STAINING buffer containing BSA (30 g/l) overnight and were
Sections (4-6 pm) of formalin fixed tissues were therafter stained with the APAAP method using
stained with or without trypsin (1-0 g/l) pretreatment polyclonal anti-LI or monoclonal Mac 387 applied as
for 10-15 minutes at 37°C. Antigen localisation was described above for ethanol-fixed tissue sections.
achieved by the alkaline phosphatase anti-alkaline Colostral IgA (2000 ng) was applied as a control
phosphatase (APAAP) method,'6 as detailed protein sample, and monoclonal anti-IgA2 was used
previously.6 Mac 387 was applied as ascitic fluid at as a control murine antibody at a dilution comparable
dilutions of 1/1200 to 1/2400 for 20 hours on formalin with that of Mac 387.
fixed sections. The latter condition could likewise be
used on ethanol fixed sections, but incubation for 30 Results
minutes at 1/400 was preferable to avoid leaching out
of cytoplasmic LI antigen. Antiserum to S-100 protein IMMUNOHISTOCHEMISTRY
was applied on formalin fixed sections at 1/1500 for 20 Mac 387 and polyclonal anti-LI applied in the
hours. After the final wash all sections were counter- APAAP method produced virtually identical staining
stained with haematoxylin. results, but Mac 387 required more appropriate
copyright.
trypsinisation of formalin fixed sections. In such
PAIRED IMMUNOFLUORESCENCE STAINING sections more extracellular LI was shown by the
A rhodamine labelled rabbit IgG (0-18 g/l) anti-LI polyclonal reagent, probably because protein antigens
conjugate was applied on ethanol fixed tissue sections are particularly masked in the interstitial matrix by
for 30 minutes and on formalin fixed sections for 20 cross linking fixatives.'8
hours. Mac 387 was used at 1/800, either mixed with Both antibody reagents produced remarkably dis-
the rhodamine conjugate or applied first in sequential tinct staining of infiltrating macrophages (fig 1).
incubations. Its reaction sites were finally shown by a Epithelioid cells were variably positive; macrophage
two step method using biotinylated horse anti-mouse giant cells were negative or only faintly stained.
IgG and fluorescein labelled avidin.'3 The red signal of Various dendritic cells were generally negative as
the anti-LI conjugate was enhanced by inclusion of described previously.6 One exception was a minor
rhodamine labelled swine anti-rabbit IgG in the last population of putative interdigitating dendritic cells in
incubation step.'3 The same detection system was used some T cell areas of lymph nodes and tonsils; paired
for paired staining with antiserum to S- 100 protein (1/ staining with Mac 387 and antiserum to S-100 protein
300) and Mac 387. The sections were evaluated in a showed a variable cell fraction with concomitant
Leitz Orthoplan microscope with a Ploem-type epi- cytoplasmic staining (fig 2). This fraction could be
illuminator. somewhat increased in dermatopathic lymphaden-
opathy.'9
IMMUNOBLOTTING EXPERIMENTS Mac 387 and polyclonal anti-LI both stained
L I protein was purified from a crude leucocyte extractnormal ora-l, pharyngeal, and vaginal squamous epi-
by preparative isoelectric focusing.' For analytical thelium in a similar pattern; normal epidermis was
focusing, LI samples (%50 pg in 15up1 water) were negative except the pilosebaceous units.6
applied near the cathode of agarose gels containing
7-5% proprietary (LKB, Sweden), pH 5 to pH 8. The COMPARATIVE TWO-COLOUR STAINING
protein bands were transferred'7 to a nitrocellulose Sequential paired immunofluorescence, with Mac 387
sheet (Bio-Rad, USA), which was subsequently cut applied before the polyclonal anti-LI, produced in all
into two equal parts. These were soaked in cases concordant staining features. Concomitant
appropriately diluted polyclonal or monoclonal green and red cytoplasmic fluorescence was seen in
antibody reagents (such as Mac 387 at 1/400) for three granulocytes and histiocytes of reactive lymph nodes,vai£g}?'
J Clin Pathol: first published as 10.1136/jcp.41.9.963 on 1 September 1988. Downloaded from http://jcp.bmj.com/ on August 31, 2023 by guest. Protected by
copyright.
Fig 3 Sequential paired immunofluorescence staining with anti-serum to Li antigen (left panel, rhodamine) and Mac
387 (right panel,fluorescein) infieldfrom a trypsinised section offormalinfixed specimen from a true histiocytic
malignant lymphoma. All neoplastic cells show concomitant labelling.
). ...
b
Fig 4 Concurrent paired bmnunofluorescence staining with antiserwn to Li antigen (left panel, rhodamine) and Mac
387 (right panel,fluorescein) infieldfrom a trypsinised section offormalinfixedspecimenfrom a true histiocytic
malignant lymphoma. Neoplastic cells show selectivefaint red staining, whereas granulocytes adjacent to vessel ( V)
show concomiiant labelling.J Clin Pathol: first published as 10.1136/jcp.41.9.963 on 1 September 1988. Downloaded from http://jcp.bmj.com/ on August 31, 2023 by guest. Protected by
Monocyte antibody specificfor LI antigen 967
copyright.
Fig 5 Concurrent paired immunofluorescence staining with antiserum to LI antigen (left panel, rhodamine) and Mac
387 (right panel,fluorescein) in a section of ethanolfixed specimen from ileal mucosa. All macrophages in Peyer's
patch show concomitant labelling. V = villus epithelium; D = dome epithelium; LF = lymphoidfollicle.
tonsils, and mucous membranes, and also in mucosal such material there was always complete concordance
squamous epithelia. Two LI positive histiocytic malig- between the two colours emitted by histiocytes sub-
nant lymphomas were likewise identically stained by jected to paired staining (fig 5).
the two reagents after sequential incubation (fig 3).
Conversely, when the two antibody reagents were ABSORPTION WITH Li ANTIGEN
mixed, concomitant fluorescence was mainly obtained When Mac 387 was absorbed with highly purified LI
where the LI antigen was present in high concentra- antigen (0-1 g/l), the staining reaction was abolished
tions, such as in granulocytes (fig 4) and squamous for both leucocytes and epithelium. This held true
epithelia. With this approach Mac 387 failed to both with formalin and ethanol fixed tonsillar sec-
decorate weakly LI-positive subpopulations of nor- tions. Only occasional granulocytes and epithelial cells
mal or malignant (fig 4) histiocytes and extracellular with a high LI concentration showed faint staining
LI antigen; the polyclonal reagent presumably had a after application of absorbed Mac 387.
greater avidity for LI and therefore partially blocked
the reactivity of Mac 387. IMMUNOBLOTTING RESULTS
Competitive inhibition of Mac 387 was not Mac 387 and polyclonal anti-LI produced identical
observed, however, when the mixed primary antibody reaction patterns when compared in Western blots
reagents were applied on ethanol fixed sections, proba- with purified Ll protein separated into various
bly because the epitope detected by the monoclonal molecular species by isoelectric focusing (fig 6). In dot
antibody was better preserved by this fixative. Thus in blots the polyclonal reagent produced a visiblet_. s.
J Clin Pathol: first published as 10.1136/jcp.41.9.963 on 1 September 1988. Downloaded from http://jcp.bmj.com/ on August 31, 2023 by guest. Protected by
968 Brandtzaeg, Jones, Flavell, Fagerhol
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.1 .e
or H C s
r
t.
.. ......
." v4..,... ...I...
.::
1.11 .. s
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zl - lglleA-; < ..
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Fig 6 Comparison of molecular patterns shown by Western Fig 7 Dot blots obtained by testing polyclonal antibody to
blotting with Mac 387 (mono mac ab) or polyclonal antibody LI antigen (poly anti-LI) or Mac 387 (mono mac ab)
copyright.
to LI antigen (poly anti-LI). Purified LI protein was against two-fold dilutions (from top to bottom) ofcrude
subjected to isoelectric focusing in agarose gel on a pH S to leucocyte extract (left lane in each panel) and two fractions
pH 8 gradient, and the protein bands were transferred to a ofpurified LI antigen (middle and right lanes). TP indicates
nitrocellulose sheet that was cut into two halves (left and total amount of appliedprotein and LI indicates amount of
right panel) before antibody incubation. specific antigen as determined by radioimmunoassay.
Identical samples were applied in left and right panels, and
the numbers show examples of the amounts of TP or LI
antigen in nanograms.
precipitate with crude leucocyte extract down to an L I
concentration of about 2 ng; the dots produced by
Mac 387 were somewhat weaker and had an end point
of about 8 ng. Parallel results were obtained with the transmembrane LI precursors released by the deter-
two purified LI fractions (fig 7). Such dots were not gent. Moreover, without adequate enzyme inhibition,
produced in the control sheets with colostral IgA or proteolysis readily takes place in leucocyte extracts.
anti-IgA2. Altogether, the immunoblotting results Another possibility is that LI behaves differently
excluded the possibility that Mac 387 reacted with an according to the available concentration of calcium
epitope that was unassociated with the LI antigen. for which it has a remarkable affinity' 5; calcium may
thus cause aggregation of LI and its binding to other
proteins. Such artefacts may not be equally expressed
Discussion for detergent extracts of granulocytes and monocytes.
The specificity of Mac 387 for the well characterised
This study showed that the monocyte antibody Mac LI antigen'35 renders this antibody a unique
387 reacts with the well defined human myelomono- immunological reagent which is now commercially
cytic LI antigen. Our conclusion is based on physico- available (Dakopatts). Previous monoclonal
chemical and immunohistochemical tests. It remains antibodies to myelomonocytic markers have been
to be explained why the molecular weights reported raised against surface antigens and have been mainly
for components detected by Mac 387 in detergent defined by staining of cell suspensions. When further
solubilised material obtained from granulocytes and characterised by immunohistochemistry, these
monocytes" were somewhat inconsistent with those antibodies have performed satisfactorily only on
previously reported for LI.' One possibility is that the cryostat sections. Moreover, they have shown striking
Mac 387 antigens to some extent might have been and unexpected specificity heterogeneity, producingJ Clin Pathol: first published as 10.1136/jcp.41.9.963 on 1 September 1988. Downloaded from http://jcp.bmj.com/ on August 31, 2023 by guest. Protected by
Monocyte antibody specific for Li antigen 969
virtually every possible combination of additional Fighting Cancer, the Norwegian Research Council for
positive staining: T and B lymphocytes,202' natural Science and the Humanities, and the Anders Jahre
killer cells,22 null cells,2' 23 platelets,23 24 and a variety of Fund.
dendritic cells.212' This is in contrast to the restricted
leucocyte distribution of the LI antigen.26 The mono- References
clonal antibody 27E10 apparently showed reactivity
with tissue macrophages and squamous epithelium 1 Dale I, Fagerhol MK, Naesgaard I. Purification and partial
similarly to Mac 387, but it was reported to detect a 17 characterization of a highly immunogenic human leukocyte
kD protein and was rarely seen in granulocytes of protein, the Ll antigen. Eur J Biochem 1983;134:1-6.
inflammatory lesions.28 Conversely, A1-3 seemed to 2 Dale 1, Brandtzaeg P, Fagerhol MK, Scott H. Distribution of a
new myelomonocytic antigen (L1) in human peripheral blood
react with tissue granulocytes and macrophages leukocytes. Immunofluorescence and immunoperoxidase stain-
similarly to Mac 387, but it was reported to detect a 52 ing features in comparison with lysozyme and lactoferrin. Am J
kD protein'and cross reacted with some fibroblasts Clin Pathol 1985;84:24-34.
and secretory epithelia.9 3 Anderson KB, Sletten K, Bemtzen HB, et al. Leukocyte LI
protein: and cystic fibrosis. Nature 1988;332:688.
Unexpected cross reactions-for example, with 4 Dorin JR, Novak M, Hill RE, Brock DJH, Secher DS, van
fibroblasts, endothelium, epithelium, and melanoma Heyningen V. A clue to the basic defect in cystic fibrosis from
cells-have, in fact, been observed by several authors cloning the CF antigen gene. Nature 987;326:614-17.
who have tested monoclonal antibodies to 5 Odink K, Cerletti N, Brulggen J, et al. Two calcium-binding
proteins in infiltrate macrophages of rheumatoid arthritis.
myelomonocytic antigens by immunohisto- Nature 1987;330:80-2.
chemistry.22 2-35 Such results, however, might be due to 6 Brandtzaeg P, Dale I, Fagerhol MK. Distribution of a formalin-
common or partially identical epitopes on different resistant myelomonocytic antigen (L1) in human tissues. 1.
molecules.6 To our knowledge LI is the first protein in Comparison with other leukocyte markers by paired immuno-
fluorescence and immunoenzyme staining. Am J Clin Pathol
addition to HLA molecules and interleukin 1,37 1987;87:681-99.
directly shown to be expressed by both squamous 7 Brandtzaeg P, Dale I, Fagerhol MK. Distribution of a formalin-
epithelium and leucocytes.7 The epithelial reactivity of resistant myelomonocytic antigen (LI) in human tissues. 2.
Mac 387 therefore has a defined molecular explana- Normal and aberrant occurrence in various epithelia. Am J Clin
Pathol 1987;87:700-7.
tion. Because of the apparent structural identity of the 8 Gabrielsen T-0, Dale I, Brandtzaeg P, et al. Epidermal and dermal
copyright.
cystic fibrosis antigen4 with the Li protein,3 epithelial distribution of a myelomonocytic antigen (L1) shared by
reactivity for the former4 likewise reflects true antigen epithelial cells in various inflammatory skin diseases. J Am Acad
expression by keratinocytes. Dermatol 1986;15: 173-9.
9 Gabrielsen T-0, Brandtzaeg P, Hoel PS, Dale I. Epithelial
As Li is a formalin resistant marker of both distribution of a myelomonocytic antigen (L1) in relation to
macrophages and squamous epithelium, Mac 387 may cutaneous malignancies and melanocytic naevi. Br J Dermatol
have several immunohistochemical applications on 1988;118:59-67.
routine pathological material. (a) L1 is excellent for 10 Isaacson PG, Jones DB. Immunohistochemical differentiation
between histiocytic and lymphoid neoplasms. Histochem J
labelling of infiltrating histiocytes in malignant lym- 1983;15:621-35.
phomas, thereby identifying cells that may confuse the 11 Flavell DJ, Jones DB, Wright DH. Identification of tissue
morphological interpretation by mimicking the neo- histiocytes on paraffin sections by a new monoclonal antibody. J
Histochem Cyochem 1987;35:1217-26.
plastic population.61' (b) By paired staining for L1 and 12 Sainte-Marie G. A paraffin-embedding technique for studies
S-100 protein'9 or HLA-DR,6 the proportion of two employing immunofluorescence. J Histochem Cytochem
types of reactive histiocytes can be determined; there 1962;I0:250-6.
are some data to indicate that such information is of 13 Brandtzaeg P, Rognum TO. Evaluation of tissue preparation
prognostic value in relation to certain neoplasms.3` methods and paired immunofluorescence staining for
immunocytochemistry of lymphomas. Histochem J
(c) Li is a useful marker of some truly histiocytic 1983;15:655-89.
tumours (figs 3-4) it has been difficult to identify all 14 Brandtzaeg P. Prolonged incubation time in immunohisto-
such malignancies by previously available phenotypic chemistry: effects on fluorescence staining of immunoglobulins
characteristics.'04' 42 (d) LI is an interesting epidermal and epithelial components in ethanol- and formaldehyde-fixed
marker in a variety of inflammatory skin diseases8 and paraffin-embedded tissues. J Histochem Cytochem
1981;29:1302-15.
skin tumours.9 (e) Li is a promising marker for 15 Takahashi K, Isobe T, Ohtsuki Y, Sonobe H, Takeda I, Akagi T.
distinction between squamous cell carcinoma and Immunohistochemical localisation and distribution of S-100
other carcinomas of the lung.43 The availability of a proteins in the human lymphoreticular system. Am J Pathol
1984;116:497-503.
monoclonal antibody to Li will hopefully facilitate 16 Mason DY. Immunohistochemical labelling of monoclonal
further immunohistochemical studies of this interest- antibodies by the APAAP immunoalkaline phosphate
ing cell marker protein. technique. In: Bullock GR, Petrusz P, eds. Immunocyto-
chemistry vol 3. London: Academic Press, 1985:25-42.
17 Norden AGW, Fulcher LM, Heys AD. Rapid typing of serum
This work was supported by grants from the Nor- paraproteins by immunoblotting without antigen-excess
wegian Cancer Society, The Norwegian Society for artifacts. Clin Chem 1987;33:1433-6.J Clin Pathol: first published as 10.1136/jcp.41.9.963 on 1 September 1988. Downloaded from http://jcp.bmj.com/ on August 31, 2023 by guest. Protected by
970 Brandtzaeg, Jones, Flavell, Fagerhol
18 Brandtzaeg P, Rognum TO. Evaluation of nine different fixatives. human mononuclear phagocytes: immunohistologic analysis
1. Preservation of immunoglobulin isotypes, J chain, and using monoclonal antibodies. Blood 1983;62:1271-9.
secretory component in human tissues. Pathol Res Pract 32 Hogg N, MacDonald S, Slusarenk M, Beverly PCL. Monoclonal
1984;179:250-66. antibodies specific for human monocytes, granulocytes and
19 Brandtzaeg P. Immunohistochemical identification of macro- endothelium. Immunology 1984;53:753-67.
phages and various dendritic cells in paraffin-embedded biopsy 33 Howie AJ, Brown G, Fisher AG, Khan M. Wide-spread
material. Acta Pathol Microbiol Immunol Scand 1988;(in press). distribution in human tissue of an antigenic determinant of
20 Hanjan SNS, Kearney JF, Cooper MD. A monoclonal antibody granulocytes. J Clin Pathol 1984;37:555-9.
(MMA) that identifies a differentiation antigen on human 34 Zwadlo G, Br6cker E-B, von Bassewitz D-B, Feige U, Sorg C. A
myelomonocytic cells. Clin Immunol Immunopathol monoclonal antibody to a differentiation antigen present on
1982;23:172-88. mature human macrophages and absent from monocytes.
21 Hirsch S, Gordon S. The use and limitation of monoclonal J Immunol 1985;134:1487-92.
antibodies against mononuclear phagocytes. Immunobiol 35 Sewell HF, Jaffray B, Thompson WD. Reaction of monoclonal
1982;161:298-307. anti Leu M 1-a myelomonocytic marker (CD1 5)-with normal
22 Ho M-K, Springer TA. Preparation and use of monoclonal anti- and neoplastic epithelia. J Pathol 1987;151:279-84.
macrophage antibodies. Methods Enzymol 1984;108:313-24. 36 Gosh S, Campbell AM. Multispecific monoclonal antibodies.
23 Talle MA, Rao PE, Westberg E, et al: Patterns of antigenic Immunol Today 1986;7:217-22.
expression on human monocytes as defined by monoclonal 37 Kupper TS, Ballard DW, Chua AO, et al. Human keratinocytes
antibodies. Cell Immunol 1983;78:83-99. contain mRNA indistinguishable from monocyte interleukin 1 a
24 Foon KA, Billing RJ, Fitchen JH, Belzer M, Drew SI, Terasaki PI. and ,B mRNA. Keratinocyte epidermal cell-derived thymocyte-
An antigen expressed by cells of the myelo-monocytic lineage. activating factor is identical to interleukin 1. J Exp Med
Am J Hematol 1981;10:259-67. 1986;164:2095-100.
25 Franklin WA, Mason DY, Pulford K, et al. Immunohistochemical 38 Nomori H, Watanabe S, Nakajima T, Shimosato Y, Kameya T.
analysis of human mononuclear phagocytes and dendritic cells Histiocytes in nasopharyngeal carcinoma in relation to
by using monoclonal antibodies. Lab Invest 1986;54:322-35. prognosis. Cancer 1986;57:100-5.
26 Hogg N, Selvendran Y. An anti-human monocyte/macrophage 39 Ree HJ, Crowley JP, Lenone LA. Macrophage-histiocytes in
monoclonal antibody, reacting most strongly with macro- malignant lymphoma, small lymphocytic type (well-differen-
phages in lymphoid tissue. Cell Immunol 1985;92:247-53. tiated lymphocytic lymphoma). Cancer 1985;56: 1117-23.
27 Seymour GJ, Poulter LW, Bofill M, et al. The reactivity of a 40 Sangster G, Crocker J, Jenkins R, Leyland MJ. Cells which
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tissues. J Reticuloendothel Soc 1983;34:463-73. 41 Isaacson PG. Histiocytic malignancy. Histopathology
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of human monocytes found only in the peripheral blood and 42 Roholl PJM, Kleyne J, Pijpers HW, van Unnik JAM.
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inflammatory tissues. J Immunol 1986;137:512-18. Comparative immunohistochemical investigation of markers
29 Hancock WW, Rickles FR, Ewan VA, Atkins RC. for malignant histiocytosis. Hum Pathol 1985;16:763-71.
Immunohistological studies with A1-3, a monoclonal antibody 43 Dale 1, Brandtzaeg P. Expression of the epithelial L1 antigen as an
to activated human monocytes and macrophages. J Immunol immunohistochemical marker of squamous cell carcinoma of
1986;136:2416-20. the lung. Histopathology (in press).
30 Flotte TJ, Springer TA, Thorbecke GJ. Dendritic cell
and macrophage staining by monoclonal antibodies in tissue
sections and epidermal sheets. Am J Pathol 1983;1 1 1:112-24. Requests for reprints to: Prof P Brandtzaeg, LIIPAT,
31 Hancock WW, Zola H, Atkins RC. Antigenic heterogeneity of Rikshospitalet, N-0027 Oslo 1, Norway.560 Book reviews
Problem Solving in Immunobematology. 3rd Notices
ed. Herbert Silver. (Pp 123; $30.) Raven
Press. 1988. ISBN 0 89189 263 X. Association of Clinical Pathologists
This excellent short book has an entertaining Junior Membership
way of presenting a wide range of problems Junior Membership of the Association of Clinical Pathologists is available to trainees
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The only omission seems to be autoimmune For Junior Membership apply to: Dr WR Timperley, Secretary, Association of
haemolysis. Each section provides a surpris- Clinical Pathologists, 57 Lower Belgrave Street, London SW1W OLR.
ing amount of information: a short introduc-
tion is followed by a series of exercises aimed
to cover the major problems likely to arise in An International Update in Dermatology and Dermatopathology
that area. The reader is invited to solve the
problems before turning to the authors' 2-5 September 1989
answers and interpretations. The book is This international meeting, jointly organised by the Pathological Society of Gt Britain
intended to develop a methodical approach and Ireland and the British Society for Dermatology, will be held at The Dome,
to blood bank problems. It succeeds admira- Brighton. Lectures and seminars will be given by a panel of invited experts. Slide
bly, is fun to use, and will be of value to both seminars will be presented by Dr Richard Reed, New Orleans, and Professor AB
clinical and laboratory haematologists. I Ackerman, New York. Abstracts are invited for poster and oral presentations. A full
thoroughly recommend it. social programme is included.
RJ SOKOL The fee is £195-00 (registration before 9 June 1989) and £225-00 after that date. Further
details from: Mrs L Barducci, British Association of Dermatologists, 6 St Andrew's
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Haematological Disorders Associated with Occupational Hazards
The Health and Safety Executive, in association with the British Society for
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Campylobacter Pylori. Ed H Menge, M Forms for this purpose and further information can be obtained from Mrs J Hopkins,
Gregor, GNJ Tytgat, BJ Marshall. (Pp 249; 7th Floor Haematology Laboratory, University of Wales College of Medicine, Heath
£30.) Springer. 1988. ISBN 3 540 18761 8. Park, Cardiff CF4 4XN.
The proceedings of a symposium on a single
organism sounds esoteric. This one is not.
It is a collection of papers and discussions The Leeds Course in Clinical Nutrition
by a select group of gastroenterologists, 5-8 September 1989 at the University of Leeds.
microbiologists, histopathologists, and Further details from: Mrs H L Helme, Department of Continued Professional
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peptic ulcer disease looked at in the light of
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This interdisciplinary approach gives a wel-
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papers include informative reviews, for 11-13 September 1989 at the Holiday Inn of Bethesda, Bethesda, Maryland
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genesis and medical management of peptic Armed Forces Institute of Pathology, Washington, DC 20306-600.
ulcer disease, and the cytoprotective action
of bismuth salts. The book is well produced,
with good photographic reproductions. Correction
There are a few phonetic misspellings of
names mentioned in the discussions but Errors were made in the text of the paper by Brandtzaeg et al J Clin Pathol 1988;41:963-70.
otherwise the text seems to be accurate. In the Material and methods section under the heading of Immunoblotting Experiments, the
Books of this sort tend to go out of date second sentence should have read: For analytical focusing, LI samples (- 50 *g in 15 p1
quickly, but this one gives sufficient ground- water) were applied near the cathode of agarose gels containing 7.5% Ampholine (LKB,
ing in the subject to maintain its interest for Sweden), pH5 to pH 8. The legend to figure 2 should have contained the following: There are
many. Like most symposium reports it is numerous S-100 protein positive, presumably interdigitating dendritic cells (left), but also
rather expensive. many cells of similar appearance labelled by Mac 387 (right). He apologises for these
MB SKIRROW oversights.You can also read
